Discovery, SAR, and X-ray structure of novel biaryl-based dipeptidyl peptidase IV inhibitors-Reference-Cited by-同舟云学术

Discovery, SAR, and X-ray structure of novel biaryl-based dipeptidyl peptidase IV inhibitors

Published:2006-01 Issue:1 Volume:16 Page:123-128
ISSN:0960-894X
Container-title:Bioorganic & Medicinal Chemistry Letters
language:en
Short-container-title:Bioorganic & Medicinal Chemistry Letters

Author:

Qiao Lei,Baumann Christian A.,Crysler Carl S.,Ninan Nisha S.,Abad Marta C.,Spurlino John C.,DesJarlais Renee L.,Kervinen Jukka,Neeper Mike P.,Bayoumy Shariff S.,Williams Robyn,Deckman Ingrid C.,Dasgupta Malini,Reed Rolanda L.,Huebert Norman D.,Tomczuk Bruce E.,Moriarty Kevin J.

Publisher

Elsevier BV

Subject

Organic Chemistry,Clinical Biochemistry,Drug Discovery,Pharmaceutical Science,Molecular Biology,Molecular Medicine,Biochemistry

Reference36 articles.

1. Glucagon-like peptides

2. Dipeptidyl Peptidase-IV CD26 in Metabolism and the Immune Response;Demuth,1995

3. Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum

4. Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide that is a major endogenous metabolite in vivo

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